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A2RXU4 (NADE_BURM9) Reviewed, UniProtKB/Swiss-Prot

Last modified December 14, 2011. Version 31. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
NH(3)-dependent NAD(+) synthetase

EC=6.3.1.5
Gene names
Name:nadE
Ordered Locus Names:BMA10229_0698
OrganismBurkholderia mallei (strain NCTC 10229) [Complete proteome] [HAMAP]
Taxonomic identifier412022 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeBurkholderiapseudomallei group

Protein attributes

Sequence length284 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

ATP + deamido-NAD+ + NH3 = AMP + diphosphate + NAD+. HAMAP MF_00193

Pathway

Cofactor biosynthesis; NAD(+) biosynthesis; NAD(+) from deamido-NAD(+) (ammonia route): step 1/1. HAMAP MF_00193

Sequence similarities

Belongs to the NAD synthetase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 284284NH(3)-dependent NAD(+) synthetase HAMAP MF_00193
PRO_1000099007

Regions

Nucleotide binding51 – 588ATP By similarity

Sites

Active site531 By similarity

Sequences

Sequence LengthMass (Da)Tools
A2RXU4 [UniParc].

Last modified March 6, 2007. Version 1.
Checksum: 8AE2C18E0B0BCEAF

FASTA28430,863
        10         20         30         40         50         60 
MSRPDQAARR RAIAAELHVS PTFDARDEAE RRIGFVADYL RTAGLRACVL GISGGIDSST 

        70         80         90        100        110        120 
AGRLAQLAVE RLRASGYDAR FVAMRLPYGA QHDEADARRA LAFVRADETL TVDVKPAADA 

       130        140        150        160        170        180 
MLAALAAGGL AYLDHAQQDF VLGNIKARER MIAQYAVAGA RNGVVIGTDH AAESVMGFFT 

       190        200        210        220        230        240 
KFGDGGADVL PLAGLTKRRV RALARMLGAD EPLVLKTPTA DLETLRPQRP DEHAYGITYE 

       250        260        270        280 
QIDDFLEGKP MDDAVAETVL RFYDATHHKR ALPYTMFDWP GHPA 

« Hide

References

[1]DeShazer D., Woods D.E., Nierman W.C.
Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: NCTC 10229.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000545 Genomic DNA. Translation: ABM99595.1.
RefSeqYP_001024513.1. NC_008835.1.

3D structure databases

ProteinModelPortalA2RXU4.
SMRA2RXU4. Positions 11-278.
ModBaseSearch...

Protein-protein interaction databases

STRINGA2RXU4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID4789317.
GenomeReviewsGene locus BMA10229_0698 in contig CP000545_GR.
KEGGbml:BMA10229_0698.
PATRIC19127905. VBIBurMal46188_0685.
TIGRBMA10229_0698.

Phylogenomic databases

HOGENOMHBG351567.
OMAIAQYEIA.
PhylomeDBA2RXU4.
ProtClustDBPRK00768.

Family and domain databases

HAMAPMF_00193. NadE.
[Tree]
InterProIPR022310. NAD/GMP_synthase.
IPR003694. NAD_synthase.
IPR022926. NH(3)-dep_NAD(+)_synth.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]
Gene3DG3DSA:3.40.50.620. Rossmann-like_a/b/a_fold. 1 hit.
KOK01916.
PfamPF02540. NAD_synthase. 1 hit.
[Graphical view]
TIGRFAMsTIGR00552. NadE. 1 hit.
ProtoNetSearch...

Entry information

Entry nameNADE_BURM9
AccessionPrimary (citable) accession number: A2RXU4
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: March 6, 2007
Last modified: December 14, 2011
This is version 31 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families